COMPARISON OF THE CATALYTIC AND INHIBITORY PROPERTIES OF PACHYSOLEN-TANNOPHILUS XYLOSE REDUCTASE TO RAT LENS ALDOSE REDUCTASE

被引：1
|
作者：
DAVIS, RA [1 ]
DERUITER, J [1 ]
机构：
[1] AUBURN UNIV,SCH PHARM,DEPT PHARMACAL SCI,DIV MED CHEM,AUBURN,AL 36849
来源：
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 1992年 / 37卷 / 01期
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D O I：
暂无
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
The catalytic and inhibitory profiles of xylose reductase isolated from the yeast Pachysolen tannophilus (PTXR) are compared to those of aldose reductase (AR) obtained form rat lens. While both PTXR and rat lens AR are NADPH-specific enzymes and have an affinity for a variety of substrates such as D-xylose, D,L-glyceraldehyde, and 4-nitrobenzaldehyde, the enzymes differ in their substrate affinity profiles. Also, PTXR is not inhibited by standard inhibitors of AR thus supporting a hypothesis that this enzyme may not possess the inhibitor binding site found in rat lens AR.
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页码：109 / 113
页数：5
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